Epidermal growth factor from the mouse. Physical evidence for a tiered beta-sheet domain: two-dimensional NMR correlated spectroscopy and nuclear Overhauser experiments on backbone amide protons.
Epidermal growth factor from the mouse. Physical evidence for a tiered beta-sheet domain: two-dimensional NMR correlated spectroscopy and nuclear Overhauser experiments on backbone amide protons.
复制标题
来自小鼠的表皮生长因子。
DOI:
10.1021/bi00335a055
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发表时间:
1985
期刊:
影响因子:
2.9
通讯作者:
Mayo,KH
中科院分区:
文献类型:
--
作者:
Mayo,KH
Revised Manuscript Received December 27, 1984 abstract: When H20-exchanged, lyophilized mouse epidermal growth factor (mEGF) is dissolved in deuterium oxideat low pH (ie, below~ 6.0), 13 well-resolved, amide proton resonances are observed in the downfield region of an NMR spectrum (500 MHz). Under the conditions of these experiments, the lifetimes of these amide protons in exchange for deuterons of the deuterium oxide solvent suggest that these amide protons are hydrogen-bonded, backbone amide protons. Several of these amide proton resonances show splittings (ie,/nho-ch) f approximately 8-10 Hz, indicating that their associated amide protons are in some type of 0-structure. Selective nuclear Overhauser effect (NOE) experiments performed on all amide proton resonances strongly suggest that all 13 of these backbone amide protons are part of a single-tiered 0-sheet structural domain in mEGF. Correlation of 2D NMR correlated spectroscopy data, identifying scaler coupled protons, with NOE data, identifying protons close to the irradiated amide protons, allows tentative assignment of some resonances in the NOE difference spectra to specific amino acid residues. These data allow a partial structural model of the tiered 0-sheet domain in mEGF to be postulated. e protein hormone, mouse epidermal growth factor (mEGF), 1 stimulates the growth and differentiation of various epidermal and epithelial tissues (Cohen, 1962, 1965; Cohen & Elliott, 1963; Turkington, 1969; Savage & Cohen, 1973). On a cellular level, mEGF works directly on skin cells by binding to a transmembrane receptor molecule and becoming f This work was supported by a grant from the National Institutes of Health (GM-34662) and by a generous gift from the Glenmede Trust Fund and benefited from NMR facilities made available to YaleUniversity through Grant CHE-7916210 from the National Science Foundation.